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Unreviewed, UniProtKB/TrEMBL O44049 (O44049_TRYRA)

Last modified June 16, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesSubmitted name:
    Sialidase EMBL AAC95493.1
    EC=3.2.1.18
OrganismTrypanosoma rangeli EMBL AAC95493.1
Taxonomic identifier5698 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

Inferred from electronic annotation. Source: InterPro

   Molecular functionexo-alpha-sialidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential EMBL AAC95493.1
Chain23 – 660638sialidase EMBL AAC95493.1
PRO_5000145206

Sequences

Sequence LengthMass (Da)Tools
O44049-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: B5D55765DC4423D0

FASTA66071,965
        10         20         30         40         50         60 
MSWLAVFVPL FLMACASEPA SALAPGSSRV ELFKRKNSTV PFEESNGTIR ERVVHSFRIP 

        70         80         90        100        110        120 
TIVNVDGVMV ATADARYETS FDNSFIETAV KYSVDDGATW NTQIAIKNSR ASSVSRVMDA 

       130        140        150        160        170        180 
TVIVKGNKLY ILVGSFNKTR NSWTQHRDGS DWEPLLVVGE VTKSAANGKT TATISWGKPV 

       190        200        210        220        230        240 
SLKPLFPAEF DGILTKEFIG GVGAAIVGSN GNLVYPVQIA DMGGRVFTKI MYSEDDGNTW 

       250        260        270        280        290        300 
KFAEGRSKFG CSEPAVLEWE GKLIINNRVD GNRRLVYESS DMGKTWVEAL GTLSHVWTNS 

       310        320        330        340        350        360 
PTSNQQDCQS SFVAVTIEGK RVMLFTHPLN LKGRWMRDRL HLWMTDNQRI FDVGQISIGD 

       370        380        390        400        410        420 
ENSGYSSVLY KDDKLYSLHE INTNDVYSLV FVRFIGELQL MKSVVRTWKE EDNHLASICT 

       430        440        450        460        470        480 
PVVPATPPSK GGCGAAVPTA GLVGFLSHSA NGSVWEDVYR CVDANVANAE RVPNGLKFNG 

       490        500        510        520        530        540 
VGGGAVWPVA RQGQTRRYQF ANYRFTLVAT VTIDELPKGT SPLLGAGLEG PGDAKLLGLS 

       550        560        570        580        590        600 
YDKNRQWRPL YGAAPASPTG SWELHKKYHV VLTMADRQGS VYVDGQPLAG SGNTVVRGAT 

       610        620        630        640        650        660 
LPDISHFYIG GPRSKGAPTD SRVTVTNIVL YNRRLNSSEI RTLFLSQDMI GTDGGAGTAA 

« Hide

References

[1]"Trypanosoma rangeli sialidase: cloning, expression and similarity to T. cruzi trans-sialidase."
Buschiazzo A., Campetella O., Frasch A.C.
Glycobiology 7:1167-1173(1997) [PubMed: 9455917] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: LDG EMBL AAC95493.1.
[2]"Structural basis of sialyltransferase activity in trypanosomal sialidases."
Buschiazzo A., Tavares G.A., Campetella O., Spinelli S., Cremona M.L., Paris G., Amaya M.F., Frasch A.C., Alzari P.M.
EMBO J. 19:16-24(2000) [PubMed: 10619840] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-660.
[3]"The high resolution structures of free and inhibitor-bound Trypanosoma rangeli sialidase and its comparison with T. cruzi trans-sialidase."
Amaya M.F., Buschiazzo A., Nguyen T., Alzari P.M.
J. Mol. Biol. 325:773-784(2003) [PubMed: 12507479] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 23-660.
[4]"A sialidase mutant displaying trans-sialidase activity."
Paris G., Ratier L., Amaya M.F., Nguyen T., Alzari P.M., Frasch A.C.
J. Mol. Biol. 345:923-934(2005) [PubMed: 15588836] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-660.
+Additional computationally mapped references.

Cross-references

Sequence databases

U83180 Genomic DNA. Translation: AAC95493.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MZ5X-ray2.20A23-660[»]
1MZ6X-ray2.90A23-660[»]
1N1SX-ray1.64A23-660[»]
1N1TX-ray1.60A23-660[»]
1N1VX-ray2.10A23-660[»]
1N1YX-ray2.80A23-660[»]
1WCSX-ray2.80A23-660[»]
2A75X-ray1.95A23-660[»]
2AGSX-ray1.70A23-660[»]
2FHRX-ray2.20A23-660[»]
ModBaseSearch...

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

Family and domain databases

InterProIPR013320. ConA-like_subgrp.
IPR008377. Sialidase_trypan.
[Graphical view]
Gene3DG3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
PRINTSPR01803. TCSIALIDASE.
ProtoNetSearch...

Entry information

Entry nameO44049_TRYRA
AccessionPrimary (citable) accession number: O44049
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: June 16, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information